In the past year we developed and published a paper on a novel apolipoprotein mimetic peptide based on apoC-II. It is a bi-helical peptide containing a class TypeA aphipathic helix as the first helix, which enables it to bind to lipoproteins. The second helix is based on the Lipoprotein Lipase (LPL) activation domain of apoC-II. The peptide showed equimolar potency in activating LPL compared to the full length apoC-II protein. We also created a novel mouse model of apoC-II deficiency, which had a hypertriglyceridemic phenotype. Treatment of the mice with the peptide lowered serum triglycerides over 90% for up to 2 days when the peptide was delivered subcutaneously. Unexpectedly the apoC-II KO mice over time became obese and insulin resistance. We are currently investigating whether increased lipolysis by apoC-II preferentially favors delivery of fatty acids to skeletal muscle. If so, it suggests that this peptide may have utility for lowering post-prandial lipids in diabetic patients. The peptide is now being licensed to an outside company.